HIF1A

From Wikipedia, the free encyclopedia


Hypoxia-inducible factor 1, alpha subunit (basic helix-loop-helix transcription factor), also known as HIF1A, is a human gene.

Hypoxia-inducible factor 1, alpha subunit (basic helix-loop-helix transcription factor)
PDB rendering based on 1h2k.
Available structures: 1h2k, 1h2l, 1h2m, 1l3e, 1l8c, 1lqb
Identifiers
Symbol(s) HIF1A; HIF-1alpha; HIF1-ALPHA; MOP1; PASD8
External IDs OMIM: 603348 MGI106918 HomoloGene1171
RNA expression pattern

More reference expression data

Orthologs
Human Mouse
Entrez 3091 15251
Ensembl ENSG00000100644 ENSMUSG00000021109
Uniprot Q16665 Q3UCW2
Refseq NM_001530 (mRNA)
NP_001521 (protein)
NM_010431 (mRNA)
NP_034561 (protein)
Location Chr 14: 61.23 - 61.28 Mb Chr 12: 74.83 - 74.87 Mb
Pubmed search [1] [2]

The protein encoded by HIF1 is a bHLH-PAS transcription factor found in mammalian cells growing at low oxygen concentrations. It plays an essential role in cellular and systemic responses to hypoxia.[1] This is one of the class of hypoxia inducible factors, a family that includes Hif1a, Hif2a, and Hif3a.

HIF1 is a heterodimer composed of Hif1a, the alpha subunit, and the aryl hydrocarbon receptor nuclear translocator (Arnt), the beta subunit. Overexpression of a natural antisense transcript (aHIF) of this gene is associated with nonpapillary renal carcinomas.[2] Two alternative transcripts encoding different isoforms have been identified.[3]

[edit] See also

[edit] References

  1. ^ Ratcliffe PJ (2003). "From erythropoietin to oxygen: hypoxia-inducible factor hydroxylases and the hypoxia signal pathway.". Blood Purif. 20 (5): 445–50. doi:10.1159/000065201. PMID 12207089. 
  2. ^ Quintero M, Mackenzie N, Brennan PA (2004). "Hypoxia-inducible factor 1 (HIF-1) in cancer.". Eur J Surg Oncol 30 (5): 465–8. doi:10.1016/j.ejso.2004.03.008. PMID 15135470. 
  3. ^ Entrez Gene: HIF1A hypoxia-inducible factor 1, alpha subunit (basic helix-loop-helix transcription factor).

[edit] Further reading

  • Semenza GL (2000). "HIF-1 and human disease: one highly involved factor.". Genes Dev. 14 (16): 1983–91. PMID 10950862. 
  • Semenza G (2002). "Signal transduction to hypoxia-inducible factor 1.". Biochem. Pharmacol. 64 (5-6): 993–8. PMID 12213597. 
  • Arbeit JM (2003). "Quiescent hypervascularity mediated by gain of HIF-1 alpha function.". Cold Spring Harb. Symp. Quant. Biol. 67: 133–42. PMID 12858534. 
  • Sitkovsky M, Lukashev D (2005). "Regulation of immune cells by local-tissue oxygen tension: HIF1 alpha and adenosine receptors.". Nat. Rev. Immunol. 5 (9): 712–21. doi:10.1038/nri1685. PMID 16110315. 
  • Mobasheri A, Richardson S, Mobasheri R, et al. (2006). "Hypoxia inducible factor-1 and facilitative glucose transporters GLUT1 and GLUT3: putative molecular components of the oxygen and glucose sensing apparatus in articular chondrocytes.". Histol. Histopathol. 20 (4): 1327–38. PMID 16136514. 
  • Schipani E (2006). "Hypoxia and HIF-1 alpha in chondrogenesis.". Semin. Cell Dev. Biol. 16 (4-5): 539–46. doi:10.1016/j.semcdb.2005.03.003. PMID 16144691. 
  • Haase VH (2006). "Hypoxia-inducible factors in the kidney.". Am. J. Physiol. Renal Physiol. 291 (2): F271–81. doi:10.1152/ajprenal.00071.2006. PMID 16554418. 
  • Liang D, Kong X, Sang N (2007). "Effects of histone deacetylase inhibitors on HIF-1.". Cell Cycle 5 (21): 2430–5. PMID 17102633.